Validation of a multidisciplinary virtual reality (VR) robotic surgical curriculum.

The objective is to identify whether trainees demonstrate improvement in a standardized knot-tying task as assessed by Global Evaluative Assessment of Robotic Skills (GEARS) score after completion of a virtual reality (VR) robotic curriculum. An IRB-exempt prospective study was conducted with surgical trainees from August 2021 to February 2023. Participants initially performed a baseline robotic suturing task in which they were instructed to tie interrupted square knots in 10 min. Participants then completed a virtual reality simulation curriculum involving 23 exercises until they achieved 90% proficiency on all tasks. Participants then repeated the suturing task. Pre- and post-curriculum suturing tasks were recorded, de-identified, and scored by expert graders using a GEARS score. Trainees from three academic centers were invited to participate. Medical students (MS1-MS3) and surgical residents from gynecology, urology, and general surgery were invited to participate. Twenty-five trainees completed the pre-curriculum suturing task, the VR curriculum, and the post-curriculum suturing task. Trainees demonstrated significant improvement in their post-test GEARS score by 2.43 points (p < 0.05) and were able to tie three additional knots within 10 min after completion of the curriculum (p < 0.05). Trainees also demonstrated a faster time to complete first knot (114 s improvement, p < 0.05) after completion of the curriculum. All participants agreed or strongly agreed that completion of the robotic curriculum helped them feel more comfortable using the robotic console, and improved their robotic surgical skills. Surgical trainees and medical students with limited prior robotic surgical experience demonstrated objective improvement after completion of a standardized VR curriculum.

Potential C-terminal-domain inhibitors of heat shock protein 90 derived from a C-terminal peptide helix.

Hsp90 is a molecular chaperone implicated in many diseases including cancer and neurodegenerative disease. Most inhibitors target the ATPase site in Hsp90's N-terminal domain, with relatively few inhibitors of other domains reported to date. Here, we show that peptides derived from a short helix at the C-terminus of Hsp90 show micromolar activity as Hsp90 inhibitors in vitro. These inhibitors do not block the N-terminal domain's ATP-binding site, and thus are likely to bind at the C-terminal domain. Substitutions and helix stapling were applied to demonstrate structure-activity relationships and improve activity. These helical peptides will help guide the design of a new class of inhibitors of Hsp90's C-terminal domain.